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| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| j.febslet.2010.07.003.pdf | 461.69 kB | Adobe PDF | 見る/開く |
| タイトル: | Origin of the pKa shift of the catalytic lysine in acetoacetate decarboxylase. |
| 著者: | Ishikita, Hiroshi |
| 著者名の別形: | 石北, 央 |
| キーワード: | Lysine pKa Acetoacetate decarboxylase Hydrophobic Solvation energy Protein dielectric |
| 発行日: | 4-Aug-2010 |
| 出版者: | Elsevier B.V. |
| 誌名: | FEBS letters |
| 巻: | 584 |
| 号: | 15 |
| 開始ページ: | 3464 |
| 終了ページ: | 3468 |
| 抄録: | The pKa value of Lys115, the catalytic residue in acetoacetate decarboxylate, was calculated using atomic coordinates of the X-ray crystal structure with consideration of the protonation states of all titratable sites in the protein. The calculated pKa value of Lys115 (pKa(Lys115)) was unusually low (approximately 6) in agreement with the experimentally measured value. Although charged residues impact pKa(Lys115) considerably in the native protein, the significant pKa(Lys115) downshift in the protein with respect to aqueous solution was mainly due to loss of the solvation energy in the catalytic active site relative to bulk water. |
| 著作権等: | © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 This is not the published version. Please cite only the published version. |
| URI: | http://hdl.handle.net/2433/169789 |
| DOI(出版社版): | 10.1016/j.febslet.2010.07.003 |
| PubMed ID: | 20621098 |
| 出現コレクション: | 学術雑誌掲載論文等 |
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